2g9l

The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction

spinqualitylabelsall models 2g9l Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2g9l is a 1 chain structure with sequence from Glandirana rugosa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 15 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GGN4_GLARU Has a non-hemolytic activity. Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria, fungi and protozoa. Publication Abstract from PubMed We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4. Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4.,Chi SW, Kim JS, Kim DH, Lee SH, Park YH, Han KH Biochem Biophys Res Commun. 2007 Jan 19;352(3):592-7. Epub 2006 Nov 27. PMID:17141187 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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